MetW regulates the enzymatic activity of MetX in Pseudomonas
| Autor: | Fumihito Hasebe |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
S-Adenosylmethionine 030106 microbiology Homoserine medicine.disease_cause Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry 03 medical and health sciences chemistry.chemical_compound Methionine Acetyltransferases medicine Amino Acid Sequence Binding site Molecular Biology Regulation of gene expression Alanine chemistry.chemical_classification Mutation Binding Sites Organic Chemistry General Medicine Amino acid 030104 developmental biology Enzyme chemistry Pseudomonas aeruginosa Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 85:351-358 |
| ISSN: | 1347-6947 |
| Popis: | Methionine is a canonical amino acid. The protein MetX is a homoserine O-acyltransferase utilized in the methionine biosynthetic pathway. The metW gene is found adjacent to the metX gene in some bacteria, but its functions are unclear. In this study, I focused on the function of MetW and MetX from Pseudomonas aeruginosa (PaMetW and PaMetX). I demonstrated that PaMetW interacted with and activated the homoserine O-succinyltransferase (HST) activity of PaMetX. Furthermore, I elucidated that the HST activity of PaMetX in complex with PaMetW was inhibited by the addition of S-adenosyl-l-homocysteine (SAH), although PaMetX alone showed no feedback inhibition. Since PaMetW possesses a glycine-rich sequence annotated as a SAM/SAH binding site, I also investigated the relationship between this glycine-rich sequence and the inhibition caused by SAH. I revealed that alanine mutation of PaMetW Gly24 reduced the inhibitory effect of SAH. These results suggest that MetW is a regulatory protein of MetX. |
| Databáze: | OpenAIRE |
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